PDBe 2p86

X-ray diffraction
1.16Å resolution

The high resolution crystal structure of rohedsain, the major cathepsin L protease from T. brucei rhodesiense, bound to inhibitor K11002

Released:
Entry authors: Brinen LS, Marion R

Function and Biology Details

Reaction catalysed:
Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine protease Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 22.9 KDa
Source organism: Trypanosoma brucei rhodesiense
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q95PM0 (Residues: 126-340; Coverage: 48%)
Gene name: rhodesain
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 33.659Å b: 78.628Å c: 80.725Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.111 0.11 0.13
Expression system: Komagataella pastoris